Selected Publication:

SHR Neuro Cancer Cardio Lipid Metab Microb

Hofer, P; Boeszoermenyi, A; Jaeger, D; Feiler, U; Arthanari, H; Mayer, N; Zehender, F; Rechberger, G; Oberer, M; Zimmermann, R; Lass, A; Haemmerle, G; Breinbauer, R; Zechner, R; Preiss-Landl, K.
Fatty Acid-binding Proteins Interact with Comparative Gene Identification-58 Linking Lipolysis with Lipid Ligand Shuttling.
J Biol Chem. 2015; 290(30):18438-18453 Doi: 10.1074/jbc.M114.628958 [OPEN ACCESS]
Web of Science PubMed FullText FullText_MUG

 

Leading authors Med Uni Graz

Hofer Peter

Altmetrics:

Dimensions Citations:

Plum Analytics:

Scite (citation analytics):

Abstract:

The coordinated breakdown of intracellular triglyceride (TG) stores requires the exquisitely regulated interaction of lipolytic enzymes with regulatory, accessory, and scaffolding proteins. Together they form a dynamic multiprotein network designated as the "lipolysome." Adipose triglyceride lipase (Atgl) catalyzes the initiating step of TG hydrolysis and requires comparative gene identification-58 (Cgi-58) as a potent activator of enzyme activity. Here, we identify adipocyte-type fatty acid-binding protein (A-Fabp) and other members of the fatty acid-binding protein (Fabp) family as interaction partners of Cgi-58. Co-immunoprecipitation, microscale thermophoresis, and solid phase assays proved direct protein/protein interaction between A-Fabp and Cgi-58. Using nuclear magnetic resonance titration experiments and site-directed mutagenesis, we located a potential contact region on A-Fabp. In functional terms, A-Fabp stimulates Atgl-catalyzed TG hydrolysis in a Cgi-58-dependent manner. Additionally, transcriptional transactivation assays with a luciferase reporter system revealed that Fabps enhance the ability of Atgl/Cgi-58-mediated lipolysis to induce the activity of peroxisome proliferator-activated receptors. Our studies identify Fabps as crucial structural and functional components of the lipolysome. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.

Find related publications in this database (using NLM MeSH Indexing)

1-Acylglycerol-3-Phosphate O-Acyltransferase - genetics

1-Acylglycerol-3-Phosphate O-Acyltransferase - metabolism

Adipose Tissue - metabolism

Animals -

COS Cells -

Chlorocebus aethiops -

Fatty Acid-Binding Proteins - genetics

Fatty Acid-Binding Proteins - metabolism

Humans -

Ligands -

Lipase - genetics

Lipase - metabolism

Lipolysis - genetics

Liposomes - metabolism

Mice -

Multiprotein Complexes - genetics

Multiprotein Complexes - metabolism

Peroxisome Proliferator-Activated Receptors - metabolism

Proteolysis -

Triglycerides - metabolism

© Med Uni Graz • Imprint